Bacterial lipids traverse the hydrophobic groove of TamB

Yiechang Lin1, Ben Corry1

  • 1Research School of Biology, Australian National University, Canberra, ACT, Australia.

Biophysical Journal
|May 16, 2026
PubMed

Insights

The TamB protein transports phospholipids across bacterial membranes via a hydrophobic groove, crucial for maintaining outer membrane integrity. This discovery sheds light on essential lipid transport mechanisms in Gram-negative bacteria.

Area of Science:

  • Microbiology
  • Molecular Biology
  • Biochemistry

Background:

  • Gram-negative bacteria possess a double-membrane envelope essential for protection.
  • Phospholipids are key components of the bacterial outer membrane (OM).
  • Mechanisms of phospholipid transport from the inner membrane (IM) to the OM are not well understood.

Purpose of the Study:

  • To investigate the role of the AsmA-like protein TamB in phospholipid transport.
  • To elucidate the structural basis of lipid transfer across bacterial membranes.

Main Methods:

  • Molecular simulations were used to model lipid transfer.
  • Interactions between TamB, TamA, and phospholipids were analyzed.
  • Structural analysis of AsmA-like proteins was performed.

Main Results:

  • TamB facilitates lipid transfer through a hydrophobic groove connecting the IM and OM.
  • Lipid release at the OM is regulated by TamA binding.
  • Other AsmA-like proteins also possess lipid-accommodating grooves.

Conclusions:

  • TamB is a key lipid transporter essential for OM integrity in Gram-negative bacteria.
  • AsmA-like proteins represent a family of potential lipid transporters.
  • Understanding these mechanisms is vital for combating bacterial infections.

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